Phosphorylation of peripherin, an intermediate filament protein, in mouse neuroblastoma nie 115 cell line and in sympathetic neurons

Huc, Claude; Escurat, Michel; Djabali, Karima; Derer, M.; Landon, Françoise; Gros, François; Portier, Marie‐Madeleine

doi:10.1016/0006-291x(89)92500-x

Cited by 26 publications

(10 citation statements)

References 38 publications

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“…Whether these differences are due to posttranslational modifications, such as phosphorylation and/or combinations of various peripherin isoforms, remains to be determined. It has been shown that peripherin can be phosphorylated (Aletta et al, 1989;Huc et al, 1989). In addition, we found that only the more acidic dimer isoform was up-regulated after axotomy.…”

Section: Discussionsupporting

confidence: 64%

Identification of a Peripherin Dimer: Changes During Axonal Development and Regeneration of the Rat Sciatic Nerve

Chadan

Moya

Portier

et al. 1994

Journal of Neurochemistry

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Western blotting of rat dorsal root ganglion (DRG) and sciatic nerve under nonreducing conditions revealed that a peripherin‐specific antibody recognized a protein species of 116/130 kDa, pi 5.6, in addition to peripherin (56 kDa, pl 5.6). We showed that this 116/130 kDa protein is a disulfide dimer of peripherin, because it gave rise to a single protein band comigrating with peripherin under reducing conditions and yielded the same proteolytic pattern as peripherin upon N‐chlorosuccinimide digestion. In addition, the immunological characteristics of the resulting peptides were identical to those of peripherin. We investigated the changes in peripherin monomer and dimer protein levels during axonal development and regeneration. During postnatal development, quantitative analysis of western blots of DRG proteins showed a significant increase in peripherin monomer (+52%) and dimer (+33%) levels from the day of birth [postnatal day 0 (PO)] to P7. The monomer levels remained high until P14 and then decreased so that at P21 and later ages, the monomer levels were similar to those observed at birth. In contrast, the dimer levels decreased continuously after P7, and in the adult, its level represented only 30% of the level at birth. Changes in [35S]methionine incorporation into adult DRG proteins were studied during regeneration of axotomized sciatic axons. Quantitative analysis of proteins showed a strong increase in labeling of both peripherin monomer (+56%) and dimer (+88%) 7 days after the crush. These levels, which remained high until 28 days after the axotomy, had returned to normal 70 days post axotomy. Our results show that peripherin monomer and dimer greatly increase during DRG fiber development and regeneration, suggesting that the two forms are involved in the growth of axons.

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Section: Discussionsupporting

confidence: 64%

Identification of a Peripherin Dimer: Changes During Axonal Development and Regeneration of the Rat Sciatic Nerve

Chadan

Moya

Portier

et al. 1994

Journal of Neurochemistry

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“…In fact, as with other intermediate filament proteins, peripherin is structured as a central coiled-coil α-helical rod domain flanked by a head and a tail domain. Head and tail domains of intermediate filament proteins are phosphorylated at several Ser/Thr sites and this has also been demonstrated for peripherin [3, 51, 55, 59]. Phosphorylation at certain sites has been shown to induce filament disassembly [53].…”

Section: Discussionmentioning

confidence: 99%

Charcot–Marie–Tooth type 2B disease-causing RAB7A mutant proteins show altered interaction with the neuronal intermediate filament peripherin

et al. 2012

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Charcot–Marie–Tooth type 2B (CMT2B) is a peripheral ulcero-mutilating neuropathy caused by four missense mutations in the rab7a gene. CMT2B is clinically characterized by prominent sensory loss, distal muscle weakness leading to muscle atrophy, high frequency of foot ulcers and infections that often results in toe amputations. RAB7A is a ubiquitous small GTPase, which controls transport to late endocytic compartments. Although the biochemical and functional properties of disease-causing RAB7A mutant proteins have been investigated, it is not yet clear how the disease originates. To understand how mutations in a ubiquitous protein specifically affect peripheral neurons, we performed a two-hybrid screen using a dorsal root ganglia cDNA library with the purpose of identifying RAB7A interactors specific for these cells. We identified peripherin, an intermediate filament protein expressed primarily in peripheral neurons, as a putative RAB7A interacting protein. The interaction was confirmed by co-immunoprecipitation and pull-down experiments, and established that the interaction is direct using recombinant proteins. Silencing or overexpression of wild type RAB7A changed the soluble/insoluble rate of peripherin indicating that RAB7A is important for peripherin organization and function. In addition, disease-causing RAB7A mutant proteins bind more strongly to peripherin and their expression causes a significant increase in the amount of soluble peripherin. Since peripherin plays a role not only in neurite outgrowth during development but also in axonal regeneration after injury, these data suggest that the altered interaction between disease-causing RAB7A mutants and peripherin could play an important role in CMT2B neuropathy.

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“…Phosphorylation sites within the intrinsically disordered head domain are associated with regulation of early steps of filament assembly; i.e., the formation of tetramers and ULFs. This has been demonstrated in several IFs, including vimentin [45,61,62], peripherin [63,64], and neurofilaments [65][66][67][68][69][70][71][72][73][74][75][76].…”

Section: Post-translational Modifications and The Functional Roles Ofmentioning

confidence: 99%

Order and disorder in intermediate filament proteins

et al. 2015

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Edited by Wilhelm Just Keywords:Intermediate filament Intrinsically disordered protein Cytoskeleton Polymer brush Self-assembly a b s t r a c t Intermediate filaments (IFs), important components of the cytoskeleton, provide a versatile, tunable network of self-assembled proteins. IF proteins contain three distinct domains: an a-helical structured rod domain, flanked by intrinsically disordered head and tail domains. Recent studies demonstrated the functional importance of the disordered domains, which differ in length and amino-acid sequence among the 70 different human IF genes. Here, we investigate the biophysical properties of the disordered domains, and review recent findings on the interactions between them. Our analysis highlights key components governing IF functional roles in the cytoskeleton, where the intrinsically disordered domains dictate protein-protein interactions, supramolecular assembly, and macro-scale order.

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Phosphorylation of peripherin, an intermediate filament protein, in mouse neuroblastoma nie 115 cell line and in sympathetic neurons

Cited by 26 publications

References 38 publications

Identification of a Peripherin Dimer: Changes During Axonal Development and Regeneration of the Rat Sciatic Nerve

Identification of a Peripherin Dimer: Changes During Axonal Development and Regeneration of the Rat Sciatic Nerve

Charcot–Marie–Tooth type 2B disease-causing RAB7A mutant proteins show altered interaction with the neuronal intermediate filament peripherin

Order and disorder in intermediate filament proteins

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